ArticleMolecular microbiology2022
Streptococcus pneumoniae binds collagens and C1q via the SSURE repeats of the PfbB adhesin.
Article in Molecular microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 9 citations in OpenAlex.
- Lactic acid bacteria-derived extracellular vesicles as postbiotic modulators of epithelial adhesion and barrier homeostasis: emerging perspectives.Frontiers in microbiology · 2026Article
- Role of endosomal toll-like receptors in immune sensing ofFrontiers in immunology · 2025Article
- Role of the SaeRS Two-Component Regulatory System in Group BMicroorganisms · 2024Article
- Article
- Engagement of αFrontiers in microbiology · 2024Article
- Characterization of Collagen Binding Activity ofPathogens (Basel, Switzerland) · 2023Article
- Antimicrobial Resistance: Two-Component Regulatory Systems and Multidrug Efflux Pumps.Antibiotics (Basel, Switzerland) · 2023Review
- C1q and central nervous system disorders.Frontiers in immunology · 2023Review
- Streptococcus pneumoniae binds collagens and C1q via the SSURE repeats of the PfbB adhesin.Molecular microbiology · 2022Article
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The binding of Streptococcus pneumoniae to collagen is likely an important step in the pathogenesis of pneumococcal infections, but little is known of the underlying molecular mechanisms. Streptococcal surface repeats (SSURE) are highly conserved protein domains present in cell wall adhesins from different Streptococcus species. We find here that SSURE repeats of the pneumococcal adhesin plasminogen and fibronectin binding protein B (PfbB) bind to various types of collagen. Moreover, deletion of the pfbB gene resulted in a significant impairment of the ability of encapsulated or unencapsulated pneumococci to bind collagen. Notably, a PfbB SSURE domain is also bound to the complement component C1q that bears a collagen-like domain and promotes adherence of pneumococci to host cells by acting as a bridge between bacteria and epithelial cells. Accordingly, deletion of PfbB or pre-treatment with anti-SSURE antibodies markedly decreased pneumococcal binding to C1q as well as C1q-dependent adherence to epithelial and endothelial cells. Further data indicated that C1q promotes pneumococcal adherence by binding to integrin α
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